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The protein encoded by DYSF belongs to the ferlin family and is a skeletal muscle protein found associated with the sarcolemma. Additionally we are shipping Dysferlin, Limb Girdle Muscular Dystrophy 2B (Autosomal Recessive) Antibodies (63) and and many more products for this protein.
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zebrafish dysferlin expression is involved in stabilizing muscle structures and its downregulation causes muscle disorganization.
dysferlin-deficient cardiomyocytes showed slower Ca2 (show CA2 ELISA Kits)+ re-sequestration. Dysferlin deficiency blunted the beta-adrenergic effect on relaxation and pumping function of ex vivo working hearts.
Using both naturally occurring and genetically engineered dysferlin-deficient mice, the authors demonstrated that loss of dysferlin confers increased susceptibility to coxsackievirus infection and myocardial damage.
By targeting DYSF premRNA introns harbouring differentially defined 3' splice sites (3' SS), we found that target introns encoding weakly defined 3' SSs were trans-spliced successfully in vitro in human myoblasts also in vivo in skeletal muscle of mice.
Dysferlin does not regulate cardiac voltage-dependent ion channels in cardiomyocytes.
results show that dysferlin exerts protective effects on the fukutin (show FKTN ELISA Kits)(Hp/-) FCMD (show FKTN ELISA Kits) mouse model, and the (dysferlin(sjl/sjl): fukutin (show FKTN ELISA Kits)(Hp/-)) mice will be useful as a novel model for a recently proposed antisense oligonucleotide therapy for FCMD (show FKTN ELISA Kits)
results provide the mechanism for dysferlin-mediated repair of skeletal muscle sarcolemma and identify ASM (show SMPD1 ELISA Kits) as a potential therapy for dysferlinopathy
These novel observations of conspicuous intermyofibrillar lipid and progressive adipocyte replacement in dysferlin-deficient muscles.
Laser-wounding induced rapid recruitment of local dysferlin-containing sarcolemma, formation of stable dysferlin accumulations surrounding lesions, endocytosis of dysferlin, and formation of large cytoplasmic vesicles from distal regions of the fiber.
Dysferlin, a calcium-triggered exocytotic membrane repair protein, is required for the cytoprotective effects of TRAF2 (show TRAF2 ELISA Kits)-mediated signaling after myocardial ischemia reperfusion injury.
Alternate splicing of the dysferlin C2A domain confers Ca(2 (show CA2 ELISA Kits)+)-dependent and Ca(2 (show CA2 ELISA Kits)+)-independent binding for membrane repair.
results support a function for dysferlin as a calcium-sensing SNARE (show NAPA ELISA Kits) effector for membrane fusion events
These differences in the structural dynamics of the predicted binding site suggest that mutation R959W alters recognition dynamics of the inner DysF domain.
This study demonstrated that novel mutation of DYSF in patient with Dysferlinopathy in Iran.
We conclude that two independent mutations in ALMS1 (show ALMS1 ELISA Kits) and DYSF cause CRD (show CRX ELISA Kits) and muscular dystrophy in the studied consanguineous Israeli Arab family.
Dysferlin carrier frequency and the number of affected individuals at risk for dysferlinopathy could be higher than previously estimated.
Our study underlines clinical heterogeneity and a high proportion of novel mutations for dysferlin in Chinese patients affected with dysferlinopathy.
Our results suggest that dysferlin protein levels of =10% in PBMCs, are highly indicative of primary dysferlinopathies
C2 domains mediate high affinity self-association of dysferlin in a parallel homodimer
dysferlin mediates lysosome fusion to the plasma membrane and thereby leads to ASMase (show SMPD1 ELISA Kits) translocation, membrane raft clustering and NADPH oxidase (show NOX1 ELISA Kits) activation in coronary arterial endothelial cells, which consequently results in endothelial dysfunction
The protein encoded by this gene belongs to the ferlin family and is a skeletal muscle protein found associated with the sarcolemma. It is involved in muscle contraction and contains C2 domains that play a role in calcium-mediated membrane fusion events, suggesting that it may be involved in membrane regeneration and repair. In addition, the protein encoded by this gene binds caveolin-3, a skeletal muscle membrane protein which is important in the formation of caveolae. Specific mutations in this gene have been shown to cause autosomal recessive limb girdle muscular dystrophy type 2B (LGMD2B) as well as Miyoshi myopathy. Alternative splicing results in multiple transcript variants.
dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)
, dysferlin variant a
, dystrophy-associated fer-1-like protein
, fer-1-like protein 1
, dystrophy-associated fer-1-like 1
, Dystrophy-associated fer-1-like protein
, Fer-1-like protein 1